Literatura científica selecionada sobre o tema "Pyrroline-5-carboxylate complex"
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Artigos de revistas sobre o assunto "Pyrroline-5-carboxylate complex"
Terao, Yukiyasu, Shigeru Nakamori e Hiroshi Takagi. "Gene Dosage Effect of l-Proline Biosynthetic Enzymes on l-Proline Accumulation and Freeze Tolerance in Saccharomyces cerevisiae". Applied and Environmental Microbiology 69, n.º 11 (novembro de 2003): 6527–32. http://dx.doi.org/10.1128/aem.69.11.6527-6532.2003.
Texto completo da fonteIon, Bogdan F., Mohamed M. Aboelnga e James W. Gauld. "Insights from molecular dynamics on substrate binding and effects of active site mutations in Δ1-pyrroline-5-carboxylate dehydrogenase". Canadian Journal of Chemistry 94, n.º 12 (dezembro de 2016): 1151–62. http://dx.doi.org/10.1139/cjc-2016-0286.
Texto completo da fonteKretz, Rita, Bita Bozorgmehr, Mohamad Hasan Kariminejad, Marianne Rohrbach, Ingrid Hausser, Alessandra Baumer, Matthias Baumgartner, Cecilia Giunta, Ariana Kariminejad e Johannes Häberle. "Defect in proline synthesis: pyrroline-5-carboxylate reductase 1 deficiency leads to a complex clinical phenotype with collagen and elastin abnormalities". Journal of Inherited Metabolic Disease 34, n.º 3 (13 de abril de 2011): 731–39. http://dx.doi.org/10.1007/s10545-011-9319-3.
Texto completo da fontePallag, Gergely, Sara Nazarian, Dora Ravasz, David Bui, Timea Komlódi, Carolina Doerrier, Erich Gnaiger, Thomas N. Seyfried e Christos Chinopoulos. "Proline Oxidation Supports Mitochondrial ATP Production When Complex I Is Inhibited". International Journal of Molecular Sciences 23, n.º 9 (4 de maio de 2022): 5111. http://dx.doi.org/10.3390/ijms23095111.
Texto completo da fonteSilao, Fitz Gerald S., Tong Jiang, Biborka Bereczky-Veress, Andreas Kühbacher, Kicki Ryman, Nathalie Uwamohoro, Sabrina Jenull et al. "Proline catabolism is a key factor facilitating Candida albicans pathogenicity". PLOS Pathogens 19, n.º 11 (2 de novembro de 2023): e1011677. http://dx.doi.org/10.1371/journal.ppat.1011677.
Texto completo da fonteLagautriere, Thomas, Ghader Bashiri e Edward N. Baker. "Use of a “silver bullet” to resolve crystal lattice dislocation disorder: A cobalamin complex of Δ1-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis". Journal of Structural Biology 189, n.º 2 (fevereiro de 2015): 153–57. http://dx.doi.org/10.1016/j.jsb.2014.12.007.
Texto completo da fonteSun, Chenglong, Tiegang Li, Xiaowei Song, Luojiao Huang, Qingce Zang, Jing Xu, Nan Bi et al. "Spatially resolved metabolomics to discover tumor-associated metabolic alterations". Proceedings of the National Academy of Sciences 116, n.º 1 (17 de dezembro de 2018): 52–57. http://dx.doi.org/10.1073/pnas.1808950116.
Texto completo da fonteYildiz, Ibrahim. "Computational insights on the hydride and proton transfer mechanisms of L-proline dehydrogenase". PLOS ONE 18, n.º 11 (15 de novembro de 2023): e0290901. http://dx.doi.org/10.1371/journal.pone.0290901.
Texto completo da fonteDelVecchio, Vito G., Joseph P. Connolly, Timothy G. Alefantis, Alexander Walz, Marian A. Quan, Guy Patra, John M. Ashton et al. "Proteomic Profiling and Identification of Immunodominant Spore Antigens of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis". Applied and Environmental Microbiology 72, n.º 9 (setembro de 2006): 6355–63. http://dx.doi.org/10.1128/aem.00455-06.
Texto completo da fonteLewoniewska, Sylwia, Ilona Oscilowska, Antonella Forlino e Jerzy Palka. "Understanding the Role of Estrogen Receptor Status in PRODH/POX-Dependent Apoptosis/Survival in Breast Cancer Cells". Biology 10, n.º 12 (10 de dezembro de 2021): 1314. http://dx.doi.org/10.3390/biology10121314.
Texto completo da fonteTeses / dissertações sobre o assunto "Pyrroline-5-carboxylate complex"
Zheng, Yao. "Identification of interacting mitochondrial enzymes involved in pyrroline-5-carboxylate metabolism in Arabidopsis thaliana". Electronic Thesis or Diss., Sorbonne université, 2021. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2021SORUS269.pdf.
Texto completo da fonteThe proteinogenic amino acid proline plays a crucial role for cellular metabolism in living organisms. In mitochondria, proline is oxidized to glutamate by the sequential action of proline dehydrogenase (ProDH) and pyrroline-5-carboxylate (P5C) dehydrogenase (P5CDH). In addition, ornithine δ-aminotransferase (δOAT) also participates in P5C formation through the conversion of ornithine and α-ketoglutarate into glutamate and P5C. Using mutants and biochemical approaches, ProDH1, P5CDH and δOAT were shown to be involved during dark-induced leaf senescence (DIS) in Arabidopsis thaliana. Striking accumulation of P5C and proline was observed in p5cdh mutant and to a lesser extent in prodh1prodh2 mutant, suggesting a putative proline-P5C cycle. Metabolomic analysis indicated that prodh1prodh2 and p5cdh have a similar metabolomic profile, but significantly different from wild-type and oat mutant, demonstrating the role of proline oxidation during DIS. ProDH1 was shown to be preferentially associated to the mitochondrial membrane fraction, while P5CDH and δOAT are more evenly distributed between matrix and membrane fractions. Homo- and hetero-oligomerizations of ProDH1, P5CDH, and δOAT were revealed using Bimolecular Fluorescence Complementation (BiFC) assay of infiltrated tobacco leaves. Interactions between P5C metabolism enzymes were further highlighted in DIS leaves using proteomics approaches coupled with mass spectrometry. Our work demonstrates that these three enzymes form P5C metabolic complex(es) involved in the oxidation of proline to fuel mitochondrial electron transfer chain to support the energy needs of senescent cells
Capítulos de livros sobre o assunto "Pyrroline-5-carboxylate complex"
Li, Peng, e Guoyao Wu. "Characteristics of Nutrition and Metabolism in Dogs and Cats". In Nutrition and Metabolism of Dogs and Cats, 55–98. Cham: Springer Nature Switzerland, 2024. http://dx.doi.org/10.1007/978-3-031-54192-6_4.
Texto completo da fonte